Mannose 6-phosphate receptor-dependent endocytosis of lysosomal enzymes is increased in sulfatide-storing kidney cells
-
Diana Klein
Abstract
Metachromatic leukodystrophy is a lysosomal disorder caused by the deficiency of arylsulfatase A (ASA). This leads to the storage of the sphingolipid 3-O-sulfogalactosylceramide (sulfatide) in various cell types, such as renal tubular cells. Examination of mannose 6-phosphate receptor (MPR300)-dependent endocytosis revealed that uptake of lysosomal enzymes is more than two-fold increased in sulfatide-storing kidney cells. Expression of MPR300 and its internalization rate is increased in these cells, whereas the recycling rate is decreased. Similar alterations can be found for the transferrin receptor, indicating that sulfatide storage leads to a general alteration of the endocytotic pathway. These data allow calculating that the endosomal pool from which receptors can recycle is 1.4- to 2-fold increased in lipid-storing cells. Immunocytochemistry demonstrates that the MPR300 in lipid-storing cells does not co-localize with accumulated sulfatide, suggesting that the kinetics of internalization and recycling appear to be altered indirectly.
©2009 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Editor's Note
- Editor's Note
- Protein Structure and Function
- Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence
- Biochemical characterization of the catalytic domains of three different clostridial collagenases
- Impact of detergents on the activity of acetylcholinesterase and on the effectiveness of its inhibitors
- The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein
- Membranes, Lipids, Glycobiology
- Glycosphingolipids from bovine milk and milk fat globule membranes: a comparative study. Adhesion to enterotoxigenic Escherichia coli strains
- Mannose 6-phosphate receptor-dependent endocytosis of lysosomal enzymes is increased in sulfatide-storing kidney cells
- Cell Biology and Signaling
- Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase
- Fibroblast growth factor 2 (FGF-2) is a novel substrate for arginine methylation by PRMT5
- Differential functions of the Apoer2 intracellular domain in selenium uptake and cell signaling
- Active immunisation against gastric inhibitory polypeptide (GIP) improves blood glucose control in an animal model of obesity-diabetes
- Novel Techniques
- Applicability of superfolder YFP bimolecular fluorescence complementation in vitro
Articles in the same Issue
- Editor's Note
- Editor's Note
- Protein Structure and Function
- Glyceryl ether monooxygenase resembles aromatic amino acid hydroxylases in metal ion and tetrahydrobiopterin dependence
- Biochemical characterization of the catalytic domains of three different clostridial collagenases
- Impact of detergents on the activity of acetylcholinesterase and on the effectiveness of its inhibitors
- The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein
- Membranes, Lipids, Glycobiology
- Glycosphingolipids from bovine milk and milk fat globule membranes: a comparative study. Adhesion to enterotoxigenic Escherichia coli strains
- Mannose 6-phosphate receptor-dependent endocytosis of lysosomal enzymes is increased in sulfatide-storing kidney cells
- Cell Biology and Signaling
- Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase
- Fibroblast growth factor 2 (FGF-2) is a novel substrate for arginine methylation by PRMT5
- Differential functions of the Apoer2 intracellular domain in selenium uptake and cell signaling
- Active immunisation against gastric inhibitory polypeptide (GIP) improves blood glucose control in an animal model of obesity-diabetes
- Novel Techniques
- Applicability of superfolder YFP bimolecular fluorescence complementation in vitro
